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Calcium in PDB 2w2o: PCSK9-Deltac D374Y Mutant Bound to Wt Egf-A of Ldlr

Protein crystallography data

The structure of PCSK9-Deltac D374Y Mutant Bound to Wt Egf-A of Ldlr, PDB code: 2w2o was solved by M.J.Bottomley, A.Cirillo, L.Orsatti, L.Ruggeri, T.S.Fisher, J.C.Santoro, R.T.Cummings, R.M.Cubbon, P.Lo Surdo, A.Calzetta, A.Noto, J.Baysarowich, M.Mattu, F.Talamo, R.De Francesco, C.P.Sparrow, A.Sitlani, A.Carfi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.62
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 85.948, 85.948, 218.329, 90.00, 90.00, 90.00
R / Rfree (%) 22.659 / 26.311

Calcium Binding Sites:

The binding sites of Calcium atom in the PCSK9-Deltac D374Y Mutant Bound to Wt Egf-A of Ldlr (pdb code 2w2o). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the PCSK9-Deltac D374Y Mutant Bound to Wt Egf-A of Ldlr, PDB code: 2w2o:

Calcium binding site 1 out of 1 in 2w2o

Go back to Calcium Binding Sites List in 2w2o
Calcium binding site 1 out of 1 in the PCSK9-Deltac D374Y Mutant Bound to Wt Egf-A of Ldlr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of PCSK9-Deltac D374Y Mutant Bound to Wt Egf-A of Ldlr within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca1333

b:93.3
occ:1.00
O E:THR294 2.4 54.5 1.0
OD2 E:ASP310 2.4 58.2 1.0
OE1 E:GLU296 2.5 59.9 1.0
O E:GLY314 2.5 59.7 1.0
O E:LEU311 2.5 56.2 1.0
C E:GLY314 3.5 60.1 1.0
C E:THR294 3.6 54.6 1.0
CD E:GLU296 3.6 59.0 1.0
CG E:ASP310 3.6 57.3 1.0
C E:LEU311 3.7 56.3 1.0
N E:GLY314 3.8 58.5 1.0
N E:LEU311 3.8 56.3 1.0
CA E:GLY314 3.8 59.3 1.0
OE2 E:GLU296 3.9 60.1 1.0
N E:THR294 4.2 54.0 1.0
OD1 E:ASP310 4.2 58.2 1.0
C E:ASP310 4.3 56.4 1.0
CA E:LEU311 4.3 56.2 1.0
O E:LYS312 4.4 56.8 1.0
CA E:THR294 4.4 54.5 1.0
N E:ASN295 4.5 54.6 1.0
CA E:ASP310 4.5 56.5 1.0
CA E:ASN295 4.5 54.9 1.0
C E:ILE313 4.6 58.0 1.0
C E:LYS312 4.6 56.9 1.0
N E:GLU296 4.6 55.1 1.0
CB E:ASP310 4.6 56.6 1.0
N E:TYR315 4.7 60.8 1.0
N E:LYS312 4.7 56.6 1.0
CG E:GLU296 4.9 57.3 1.0
O E:ALA291 4.9 52.6 1.0
O E:ASP310 5.0 56.8 1.0
CB E:TYR315 5.0 61.3 1.0
CA E:LYS312 5.0 56.9 1.0
CB E:THR294 5.0 54.5 1.0

Reference:

M.J.Bottomley, A.Cirillo, L.Orsatti, L.Ruggeri, T.S.Fisher, J.C.Santoro, R.T.Cummings, R.M.Cubbon, P.Lo Surdo, A.Calzetta, A.Noto, J.Baysarowich, M.Mattu, F.Talamo, R.De Francesco, C.P.Sparrow, A.Sitlani, A.Carfi. Structural and Biochemical Characterization of the Wild Type PCSK9/Egf-Ab Complex and Natural Fh Mutants. J.Biol.Chem. V. 284 1313 2009.
ISSN: ISSN 0021-9258
PubMed: 19001363
DOI: 10.1074/JBC.M808363200
Page generated: Sat Dec 12 03:55:01 2020

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